RPC1_LAMBD
ID RPC1_LAMBD Reviewed; 237 AA.
AC P03034;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 153.
DE RecName: Full=Repressor protein cI;
GN Name=cI; OrderedLocusNames=lambdap88;
OS Escherichia phage lambda (Bacteriophage lambda).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT "Nucleotide sequence of bacteriophage lambda DNA.";
RL J. Mol. Biol. 162:729-773(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=714163; DOI=10.1038/276301a0;
RA Sauer R.T.;
RT "DNA sequence of the bacteriophage gama cI gene.";
RL Nature 276:301-302(1978).
RN [3]
RP PROTEIN SEQUENCE OF 2-237.
RX PubMed=629949; DOI=10.1021/bi00599a024;
RA Sauer R.T., Anderegg R.;
RT "Primary structure of the lambda repressor.";
RL Biochemistry 17:1092-1100(1978).
RN [4]
RP FUNCTION, AND OLIGOMERIZATION.
RX PubMed=11711436; DOI=10.1101/gad.937301;
RA Dodd I.B., Perkins A.J., Tsemitsidis D., Egan J.B.;
RT "Octamerization of lambda CI repressor is needed for effective repression
RT of P(RM) and efficient switching from lysogeny.";
RL Genes Dev. 15:3013-3022(2001).
RN [5]
RP REVIEW ON FUNCTION.
RX PubMed=19181516; DOI=10.1016/j.sbi.2008.12.008;
RA Hochschild A., Lewis M.;
RT "The bacteriophage lambda CI protein finds an asymmetric solution.";
RL Curr. Opin. Struct. Biol. 19:79-86(2009).
RN [6]
RP FUNCTION.
RX PubMed=21873207; DOI=10.1073/pnas.1111221108;
RA Lewis D., Le P., Zurla C., Finzi L., Adhya S.;
RT "Multilevel autoregulation of lambda repressor protein CI by DNA looping in
RT vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:14807-14812(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-93.
RX PubMed=6226802; DOI=10.1016/s0022-2836(83)80169-7;
RA Ohlendorf D.H., Anderson W.F., Lewis M., Pabo C.O., Matthews B.W.;
RT "Comparison of the structures of cro and lambda repressor proteins from
RT bacteriophage lambda.";
RL J. Mol. Biol. 169:757-769(1983).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-93.
RX PubMed=3187530; DOI=10.1126/science.3187530;
RA Jordan S.R., Pabo C.O.;
RT "Structure of the lambda complex at 2.5-A resolution: details of the
RT repressor-operator interactions.";
RL Science 242:893-898(1988).
CC -!- FUNCTION: Acts as a transcriptional repressor that allows virus to
CC establish and maintain latency. Prevents both the viral DNA replication
CC and the exit programs. Clamps the two operator OL (operator left made
CC of OL1, OL2 and OL3 sites) and OR (operator right made of OR1, OR2 and
CC OR3 sites) together by binding to them and arranging the intervening
CC DNA in a loop. This step allows repression of lytic pR and pL promoters
CC by binding to OL1, OL2, OR1 and OR2 simultaneously. The binding of cI
CC on OR2 additionally activates the transcription of the cI gene thereby
CC mediating an autoregulatory function to maintain the latent state. Once
CC cI is present in sufficient amount, it can repress its own
CC transcription by binding to OL3 and OR3. {ECO:0000269|PubMed:11711436,
CC ECO:0000269|PubMed:21873207}.
CC -!- SUBUNIT: Homooctamer. The DNA loop is maintained by octamers of
CC repressor cI.
CC -!- INTERACTION:
CC P03034; P03034: cI; NbExp=2; IntAct=EBI-4478303, EBI-4478303;
CC -!- MISCELLANEOUS: Bacterial cells harboring a lysogenic lambda phage are
CC immune to further infection by lambda. The cI repressor protein
CC inhibits the lytic development of any additional infecting phage
CC particles. The region of the genome that codes for the cI repressor
CC protein is known as the immunity region.
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DR EMBL; J02459; AAA96581.1; -; Genomic_DNA.
DR EMBL; X00166; CAA24991.1; -; Genomic_DNA.
DR PIR; A14086; RPBPL.
DR RefSeq; NP_040628.1; NC_001416.1.
DR PDB; 1F39; X-ray; 1.90 A; A/B=137-237.
DR PDB; 1KCA; X-ray; 2.91 A; A/B/C/D/E/F/G/H=133-237.
DR PDB; 1LLI; X-ray; 2.10 A; A/B=2-93.
DR PDB; 1LMB; X-ray; 1.80 A; 3/4=2-93.
DR PDB; 1LRP; X-ray; 3.20 A; A/B/C=2-93.
DR PDB; 1RIO; X-ray; 2.30 A; A/B=1-92.
DR PDB; 3BDN; X-ray; 3.91 A; A/B=2-237.
DR PDB; 3KZ3; X-ray; 1.64 A; A/B=8-85.
DR PDB; 3WOA; X-ray; 2.00 A; A=1-46.
DR PDB; 5ZCA; X-ray; 1.80 A; A=1-21.
DR PDB; 7JVT; X-ray; 3.16 A; C/D=1-93.
DR PDBsum; 1F39; -.
DR PDBsum; 1KCA; -.
DR PDBsum; 1LLI; -.
DR PDBsum; 1LMB; -.
DR PDBsum; 1LRP; -.
DR PDBsum; 1RIO; -.
DR PDBsum; 3BDN; -.
DR PDBsum; 3KZ3; -.
DR PDBsum; 3WOA; -.
DR PDBsum; 5ZCA; -.
DR PDBsum; 7JVT; -.
DR SMR; P03034; -.
DR DIP; DIP-17006N; -.
DR IntAct; P03034; 2.
DR MEROPS; S24.002; -.
DR GeneID; 2703537; -.
DR GeneID; 2703538; -.
DR KEGG; vg:3827059; -.
DR EvolutionaryTrace; P03034; -.
DR Proteomes; UP000001711; Genome.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:CAFA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0098689; P:latency-replication decision; IEA:UniProtKB-KW.
DR GO; GO:0019044; P:maintenance of viral latency; IMP:CAFA.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IDA:CAFA.
DR GO; GO:0050434; P:positive regulation of viral transcription; IDA:CAFA.
DR CDD; cd00093; HTH_XRE; 1.
DR CDD; cd06529; S24_LexA-like; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR039418; LexA-like.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR015927; Peptidase_S24_S26A/B/C.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF00717; Peptidase_S24; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR SUPFAM; SSF51306; SSF51306; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA-binding;
KW Latency-replication decision; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Viral latency;
KW Viral latency initiation and maintenance.
FT INIT_MET 1
FT /note="Removed; by host"
FT /evidence="ECO:0000269|PubMed:629949"
FT CHAIN 2..237
FT /note="Repressor protein cI"
FT /id="PRO_0000149715"
FT DOMAIN 19..77
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 30..49
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT CONFLICT 67
FT /note="A -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="E -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
FT HELIX 10..30
FT /evidence="ECO:0007829|PDB:3KZ3"
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:3KZ3"
FT HELIX 45..52
FT /evidence="ECO:0007829|PDB:3KZ3"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:3KZ3"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3KZ3"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:3KZ3"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1LMB"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1F39"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1F39"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:1F39"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:1F39"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1F39"
FT STRAND 221..230
FT /evidence="ECO:0007829|PDB:1F39"
FT HELIX 233..236
FT /evidence="ECO:0007829|PDB:1F39"
SQ SEQUENCE 237 AA; 26212 MW; 4785A4915479ED97 CRC64;
MSTKKKPLTQ EQLEDARRLK AIYEKKKNEL GLSQESVADK MGMGQSGVGA LFNGINALNA
YNAALLAKIL KVSVEEFSPS IAREIYEMYE AVSMQPSLRS EYEYPVFSHV QAGMFSPELR
TFTKGDAERW VSTTKKASDS AFWLEVEGNS MTAPTGSKPS FPDGMLILVD PEQAVEPGDF
CIARLGGDEF TFKKLIRDSG QVFLQPLNPQ YPMIPCNESC SVVGKVIASQ WPEETFG
